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Volumn 289, Issue 36, 2014, Pages 24771-24778

Agonist ligands mediate the transcriptional response of nuclear receptor heterodimers through distinct stoichiometric assemblies with coactivators

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; MOLECULES; PROTEINS; TRANSCRIPTION; X RAY SCATTERING;

EID: 84906960108     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.575423     Document Type: Article
Times cited : (13)

References (60)
  • 1
    • 0035813090 scopus 로고    scopus 로고
    • Coregulator codes of transcriptional regulation by nuclear receptors
    • Rosenfeld, M. G., and Glass, C. K. (2001) Coregulator codes of transcriptional regulation by nuclear receptors. J. Biol. Chem. 276, 36865-36868
    • (2001) J. Biol. Chem. , vol.276 , pp. 36865-36868
    • Rosenfeld, M.G.1    Glass, C.K.2
  • 3
    • 84879086561 scopus 로고    scopus 로고
    • Allosteric controls of nuclear receptor function in the regulation of transcription
    • Billas, I., and Moras, D. (2013) Allosteric controls of nuclear receptor function in the regulation of transcription. J. Mol. Biol. 425, 2317-2329
    • (2013) J. Mol. Biol. , vol.425 , pp. 2317-2329
    • Billas, I.1    Moras, D.2
  • 4
    • 0032524634 scopus 로고    scopus 로고
    • The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors
    • Onate, S. A., Boonyaratanakornkit, V., Spencer, T. E., Tsai, S. Y., Tsai, M. J., Edwards, D. P., and O'Malley, B. W. (1998) The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J. Biol. Chem. 273, 12101-12108
    • (1998) J. Biol. Chem. , vol.273 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3    Tsai, S.Y.4    Tsai, M.J.5    Edwards, D.P.6    O'Malley, B.W.7
  • 5
    • 1642304065 scopus 로고    scopus 로고
    • Structural determinants of allosteric ligand activation in RXR heterodimers
    • Shulman, A. I., Larson, C., Mangelsdorf, D. J., and Ranganathan, R. (2004) Structural determinants of allosteric ligand activation in RXR heterodimers. Cell 116, 417-429
    • (2004) Cell , vol.116 , pp. 417-429
    • Shulman, A.I.1    Larson, C.2    Mangelsdorf, D.J.3    Ranganathan, R.4
  • 6
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • Forman, B. M., Umesono, K., Chen, J., and Evans, R. M. (1995) Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81, 541-550
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, J.3    Evans, R.M.4
  • 7
    • 84859982562 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity within agonist-bound TR:RXR heterodimers
    • Putcha, B. D., Wright, E., Brunzelle, J. S., and Fernandez, E. J. (2012) Structural basis for negative cooperativity within agonist-bound TR:RXR heterodimers. Proc. Natl. Acad. Sci. U.S.A. 109, 6084-6087
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 6084-6087
    • Putcha, B.D.1    Wright, E.2    Brunzelle, J.S.3    Fernandez, E.J.4
  • 9
    • 0034687397 scopus 로고    scopus 로고
    • The nuclear receptor CAR mediates specific xenobiotic induction of drug metabolism
    • Wei, P., Zhang, J., Egan-Hafley, M., Liang, S., and Moore, D. D. (2000) The nuclear receptor CAR mediates specific xenobiotic induction of drug metabolism. Nature 407, 920-923
    • (2000) Nature , vol.407 , pp. 920-923
    • Wei, P.1    Zhang, J.2    Egan-Hafley, M.3    Liang, S.4    Moore, D.D.5
  • 10
    • 0037064177 scopus 로고    scopus 로고
    • Modulation of acetaminophen-induced hepatotoxicity by the xenobiotic receptor CAR
    • Zhang, J., Huang, W., Chua, S. S., Wei, P., and Moore, D. D. (2002) Modulation of acetaminophen-induced hepatotoxicity by the xenobiotic receptor CAR. Science 298, 422-424
    • (2002) Science , vol.298 , pp. 422-424
    • Zhang, J.1    Huang, W.2    Chua, S.S.3    Wei, P.4    Moore, D.D.5
  • 11
    • 0037303706 scopus 로고    scopus 로고
    • A nuclear receptor-mediated xenobiotic response and its implication in drug metabolism and host protection
    • Sonoda, J., Rosenfeld, J. M., Xu, L., Evans, R. M., and Xie, W. (2003) A nuclear receptor-mediated xenobiotic response and its implication in drug metabolism and host protection. Curr. Drug Metab. 4, 59-72
    • (2003) Curr. Drug Metab. , vol.4 , pp. 59-72
    • Sonoda, J.1    Rosenfeld, J.M.2    Xu, L.3    Evans, R.M.4    Xie, W.5
  • 13
    • 0028210426 scopus 로고
    • A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements
    • Baes, M., Gulick, T., Choi, H. S., Martinoli, M. G., Simha, D., and Moore, D. D. (1994) A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol. Cell. Biol. 14, 1544-1552
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1544-1552
    • Baes, M.1    Gulick, T.2    Choi, H.S.3    Martinoli, M.G.4    Simha, D.5    Moore, D.D.6
  • 14
    • 0030802649 scopus 로고    scopus 로고
    • Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR
    • Choi, H. S., Chung, M., Tzameli, I., Simha, D., Lee, Y. K., Seol, W., and Moore, D. D. (1997) Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR. J. Biol. Chem. 272, 23565-23571
    • (1997) J. Biol. Chem. , vol.272 , pp. 23565-23571
    • Choi, H.S.1    Chung, M.2    Tzameli, I.3    Simha, D.4    Lee, Y.K.5    Seol, W.6    Moore, D.D.7
  • 15
    • 0036311095 scopus 로고    scopus 로고
    • A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity
    • Dussault, I., Lin, M., Hollister, K., Fan, M., Termini, J., Sherman, M. A., and Forman, B. M. (2002) A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity. Mol. Cell. Biol. 22, 5270-5280
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5270-5280
    • Dussault, I.1    Lin, M.2    Hollister, K.3    Fan, M.4    Termini, J.5    Sherman, M.A.6    Forman, B.M.7
  • 16
    • 10944250224 scopus 로고    scopus 로고
    • The nuclear xenobiotic receptor CAR: Structural determinants of constitutive activation and heterodimerization
    • Suino, K., Peng, L., Reynolds, R., Li, Y., Cha, J. Y., Repa, J. J., Kliewer, S. A., and Xu, H. E. (2004) The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization. Mol. Cell 16, 893-905
    • (2004) Mol. Cell , vol.16 , pp. 893-905
    • Suino, K.1    Peng, L.2    Reynolds, R.3    Li, Y.4    Cha, J.Y.5    Repa, J.J.6    Kliewer, S.A.7    Xu, H.E.8
  • 18
    • 0033999734 scopus 로고    scopus 로고
    • The xenobiotic compound 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene is an agonist ligand for the nuclear receptor CAR
    • Tzameli, I., Pissios, P., Schuetz, E. G., and Moore, D. D. (2000) The xenobiotic compound 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene is an agonist ligand for the nuclear receptor CAR. Mol. Cell. Biol. 20, 2951-2958
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2951-2958
    • Tzameli, I.1    Pissios, P.2    Schuetz, E.G.3    Moore, D.D.4
  • 22
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao, T. P., Ku, G., Zhou, N., Scully, R., and Livingston, D. M. (1996) The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl. Acad. Sci. U.S.A. 93, 10626-10631
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10626-10631
    • Yao, T.P.1    Ku, G.2    Zhou, N.3    Scully, R.4    Livingston, D.M.5
  • 24
    • 33846418778 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction between CAR-RXR and SRC-1 peptide by isothermal titration calorimetry
    • Wright, E., Vincent, J., and Fernandez, E. J. (2007) Thermodynamic characterization of the interaction between CAR-RXR and SRC-1 peptide by isothermal titration calorimetry. Biochemistry 46, 862-870
    • (2007) Biochemistry , vol.46 , pp. 862-870
    • Wright, E.1    Vincent, J.2    Fernandez, E.J.3
  • 26
  • 27
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 28
    • 84857132923 scopus 로고    scopus 로고
    • How random are intrinsically disordered proteins? A small angle scattering perspective
    • Receveur-Brechot, V., and Durand, D. (2012) How random are intrinsically disordered proteins? A small angle scattering perspective. Curr. Protein Pept. Sci. 13, 55-75
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 55-75
    • Receveur-Brechot, V.1    Durand, D.2
  • 29
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • Rambo, R. P., and Tainer, J. A. (2013) Accurate assessment of mass, models and resolution by small-angle scattering. Nature 496, 477-481
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 30
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 32
    • 84870267223 scopus 로고
    • The generalization of students problem when several different population variances are involved
    • Welch, B. L. (1947) The generalization of students problem when several different population variances are involved. Biometrika 34, 28-35
    • (1947) Biometrika , vol.34 , pp. 28-35
    • Welch, B.L.1
  • 34
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo, C., and Chen, J. D. (2000) The SRC family of nuclear receptor coactivators. Gene 245, 1-11
    • (2000) Gene , vol.245 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 35
    • 84866607246 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Modulators of pathology and therapeutic targets
    • Lonard, D. M., and O'Malley, B. W. (2012) Nuclear receptor coregulators: modulators of pathology and therapeutic targets. Nat. Rev. Endocrinol. 8, 598-604
    • (2012) Nat. Rev. Endocrinol. , vol.8 , pp. 598-604
    • Lonard, D.M.1    O'Malley, B.W.2
  • 36
    • 84887338695 scopus 로고    scopus 로고
    • An evolving understanding of nuclear receptor coregulator proteins
    • Millard, C. J., Watson, P. J., Fairall, L., and Schwabe, J. W. (2013) An evolving understanding of nuclear receptor coregulator proteins. J. Mol. Endocrinol. 51, T23-T36
    • (2013) J. Mol. Endocrinol. , vol.51 , pp. T23-T36
    • Millard, C.J.1    Watson, P.J.2    Fairall, L.3    Schwabe, J.W.4
  • 37
    • 82655174048 scopus 로고    scopus 로고
    • Steroid receptor coactivators 1, 2, and 3: Critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy
    • Johnson, A. B., and O'Malley, B. W. (2012) Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy. Mol. Cell Endocrinol. 348, 430-439
    • (2012) Mol. Cell Endocrinol. , vol.348 , pp. 430-439
    • Johnson, A.B.1    O'Malley, B.W.2
  • 39
    • 0029085038 scopus 로고
    • Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation
    • Schulman, I. G., Chakravarti, D., Juguilon, H., Romo, A., and Evans, R. M. (1995) Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. U.S.A. 92, 8288-8292
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8288-8292
    • Schulman, I.G.1    Chakravarti, D.2    Juguilon, H.3    Romo, A.4    Evans, R.M.5
  • 40
    • 0031043055 scopus 로고    scopus 로고
    • The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor
    • Schulman, I. G., Li, C., Schwabe, J. W., and Evans, R. M. (1997) The phantom ligand effect: allosteric control of transcription by the retinoid X receptor. Genes Dev. 11, 299-308
    • (1997) Genes Dev. , vol.11 , pp. 299-308
    • Schulman, I.G.1    Li, C.2    Schwabe, J.W.3    Evans, R.M.4
  • 42
    • 41249102742 scopus 로고    scopus 로고
    • Ab initio fragment molecular orbital study of molecular interactions between liganded retinoid X receptor and its coactivator; part II: Influence of mutations in transcriptional activation function 2 activating domain core on the molecular interactions
    • Ito, M., Fukuzawa, K., Mochizuki, Y., Nakano, T., and Tanaka, S. (2008) Ab initio fragment molecular orbital study of molecular interactions between liganded retinoid X receptor and its coactivator; part II: influence of mutations in transcriptional activation function 2 activating domain core on the molecular interactions. J. Phys. Chem. A 112, 1986-1998
    • (2008) J. Phys. Chem. A , vol.112 , pp. 1986-1998
    • Ito, M.1    Fukuzawa, K.2    Mochizuki, Y.3    Nakano, T.4    Tanaka, S.5
  • 43
    • 0037050017 scopus 로고    scopus 로고
    • Co-regulator recruitment and the mechanism of retinoic acid receptor synergy
    • Germain, P., Iyer, J., Zechel, C., and Gronemeyer, H. (2002) Co-regulator recruitment and the mechanism of retinoic acid receptor synergy. Nature 415, 187-192
    • (2002) Nature , vol.415 , pp. 187-192
    • Germain, P.1    Iyer, J.2    Zechel, C.3    Gronemeyer, H.4
  • 46
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., Kalkhoven, E., Hoare, S., and Parker, M. G. (1997) A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387, 733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 47
    • 0032472408 scopus 로고    scopus 로고
    • Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor
    • Kalkhoven, E., Valentine, J. E., Heery, D. M., and Parker, M. G. (1998) Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17, 232-243
    • (1998) EMBO J. , vol.17 , pp. 232-243
    • Kalkhoven, E.1    Valentine, J.E.2    Heery, D.M.3    Parker, M.G.4
  • 48
    • 0027237598 scopus 로고
    • Determinants for selective RAR and TR recognition of direct repeat HREs
    • Perlmann, T., Rangarajan, P. N., Umesono, K., and Evans, R. M. (1993) Determinants for selective RAR and TR recognition of direct repeat HREs. Genes Dev. 7, 1411-1422
    • (1993) Genes Dev. , vol.7 , pp. 1411-1422
    • Perlmann, T.1    Rangarajan, P.N.2    Umesono, K.3    Evans, R.M.4
  • 49
    • 0027202156 scopus 로고
    • Differential orientations of the DNA-binding domain and carboxyl-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers
    • Kurokawa, R., Yu, V. C., Näär, A., Kyakumoto, S., Han, Z., Silverman, S., Rosenfeld, M. G., and Glass, C. K. (1993) Differential orientations of the DNA-binding domain and carboxyl-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers. Genes Dev. 7, 1423-1435
    • (1993) Genes Dev. , vol.7 , pp. 1423-1435
    • Kurokawa, R.1    Yu, V.C.2    Näär, A.3    Kyakumoto, S.4    Han, Z.5    Silverman, S.6    Rosenfeld, M.G.7    Glass, C.K.8
  • 50
    • 0028313996 scopus 로고
    • The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats
    • Zechel, C., Shen, X. Q., Chen, J. Y., Chen, Z. P., Chambon, P., and Gronemeyer, H. (1994) The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats. EMBO J. 13, 1425-1433
    • (1994) EMBO J. , vol.13 , pp. 1425-1433
    • Zechel, C.1    Shen, X.Q.2    Chen, J.Y.3    Chen, Z.P.4    Chambon, P.5    Gronemeyer, H.6
  • 51
    • 0037570621 scopus 로고    scopus 로고
    • Progesterone and glucocorticoid receptors recruit distinct coactivator complexes and promote distinct patterns of local chromatin modification
    • Li, X., Wong, J., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W. (2003) Progesterone and glucocorticoid receptors recruit distinct coactivator complexes and promote distinct patterns of local chromatin modification. Mol. Cell. Biol. 23, 3763-3773
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3763-3773
    • Li, X.1    Wong, J.2    Tsai, S.Y.3    Tsai, M.J.4    O'Malley, B.W.5
  • 54
    • 35348969404 scopus 로고    scopus 로고
    • Targeting PGC-1 α to control energy homeostasis
    • Wu, Z., and Boss, O. (2007) Targeting PGC-1 α to control energy homeostasis. Expert. Opin. Ther. Targets 11, 1329-1338
    • (2007) Expert. Opin. Ther. Targets , vol.11 , pp. 1329-1338
    • Wu, Z.1    Boss, O.2
  • 55
    • 84863230611 scopus 로고    scopus 로고
    • Synthesis and evaluation of sulfonylnitrophenylthiazoles (SNPTs) as thyroid hormone receptor-coactivator interaction inhibitors
    • Hwang, J. Y., Attia, R. R., Zhu, F., Yang, L., Lemoff, A., Jeffries, C., Connelly, M. C., and Guy, R. K. (2012) Synthesis and evaluation of sulfonylnitrophenylthiazoles (SNPTs) as thyroid hormone receptor-coactivator interaction inhibitors. J. Med. Chem. 55, 2301-2310
    • (2012) J. Med. Chem. , vol.55 , pp. 2301-2310
    • Hwang, J.Y.1    Attia, R.R.2    Zhu, F.3    Yang, L.4    Lemoff, A.5    Jeffries, C.6    Connelly, M.C.7    Guy, R.K.8
  • 56
    • 0032230231 scopus 로고    scopus 로고
    • Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): Multiple motifs with different binding specificities
    • Ding, X. F., Anderson, C. M., Ma, H., Hong, H., Uht, R. M., Kushner, P. J., and Stallcup, M. R. (1998) Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Mol. Endocrinol. 12, 302-313
    • (1998) Mol. Endocrinol. , vol.12 , pp. 302-313
    • Ding, X.F.1    Anderson, C.M.2    Ma, H.3    Hong, H.4    Uht, R.M.5    Kushner, P.J.6    Stallcup, M.R.7
  • 59
    • 4043140077 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain
    • Lengqvist, J., Mata De Urquiza, A., Bergman, A. C., Willson, T. M., Sjövall, J., Perlmann, T., and Griffiths, W. J. (2004) Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain. Mol. Cell Proteomics 3, 692-703
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 692-703
    • Lengqvist, J.1    Mata De Urquiza, A.2    Bergman, A.C.3    Willson, T.M.4    Sjövall, J.5    Perlmann, T.6    Griffiths, W.J.7
  • 60
    • 70450252023 scopus 로고    scopus 로고
    • NR4A orphan nuclear receptors influence retinoic acid and docosahexaenoic acid signaling via up-regulation of fatty acid binding protein 5
    • Volakakis, N., Joodmardi, E., and Perlmann, T. (2009) NR4A orphan nuclear receptors influence retinoic acid and docosahexaenoic acid signaling via up-regulation of fatty acid binding protein 5. Biochem. Biophys. Res. Commun. 390, 1186-1191
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1186-1191
    • Volakakis, N.1    Joodmardi, E.2    Perlmann, T.3


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